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Literature summary extracted from

  • Stojanovski, B.M.; Hunter, G.A.; Jahn, M.; Jahn, D.; Ferreira, G.C.
    Unstable reaction intermediates and hysteresis during the catalytic cycle of 5-aminolevulinate synthase: implications from using pseudo and alternate substrates and a promiscuous enzyme variant (2014), J. Biol. Chem., 289, 22915-22925.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.37 T148A site-directed mutagenesis, the active site Thr148 mutation modulates the enzyme's strict amino acid substrate specificity Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.37 additional information
-
additional information pre-steady state and steady state kinetics, overview Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.37 succinyl-CoA + glycine Mus musculus
-
5-aminolevulinate + CoA + CO2
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.37 Mus musculus P08680
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 the rate of 5-aminolevulinate release is controlled by a hysteretic kinetic mechanism initiated by conformational changes of the enzyme. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity. Catalytic mechanism, overview Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.37 additional information analysis of unstable enzyme-catalyzed reaction intermediates and conformational changes using physiological and non-physiological substrates and promiscuous T148A enzyme variant, overview. Formation of the quinonoid intermediate upon reacting glycine with the enzyme. Significantly, in the absence of the succinyl-CoA substrate, the external aldimine predominates over the glycine quinonoid intermediate. When instead of glycine, L-serine is reacted with the enzyme, a lag phase is observed in the progress curve for the L-serine external aldimine formation, indicating a hysteretic behavior in enzyme ALAS. Hysteresis is not detected in the T148A-catalyzed L-serine external aldimine formation. The rate of 5-aminolevulinate release is also controlled by a hysteretic kinetic mechanism. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity, positioning of the glycine external aldimine in the active site, overview Mus musculus ?
-
?
2.3.1.37 succinyl-CoA + glycine
-
Mus musculus 5-aminolevulinate + CoA + CO2
-
r
2.3.1.37 succinyl-CoA + L-serine the reaction with L-serine follows a biphasic kinetic process Mus musculus ?
-
?
2.3.1.37 succinyl-CoA + O-methylglycine
-
Mus musculus ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.37 18
-
assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.37 7.5
-
assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.37 pyridoxal 5'-phosphate dependent on Mus musculus

General Information

EC Number General Information Comment Organism
2.3.1.37 metabolism 5-aminolevulinate synthase catalyzs the initial step of mammalian heme biosynthesis Mus musculus